Publication date
18/06/2014Author
Mabb, A.M.Je, H.S.
Wall, M.J.
Robinson, C.G.
Larsen, R.S.
Qiang, Y.
Corrêa, Sonia A.L.
Ehlers, M.D.
Keyword
Triad3ARegulation
Synaptic strength
Arc induction
Ubiquitination
Glutamatergic synapses
Synaptic plasticity
Peer-Reviewed
YesOpen Access status
closedAccessAccepted for publication
02/05/2014
Metadata
Show full item recordAbstract
Activity-dependent gene transcription and protein synthesis underlie many forms of learning-related synaptic plasticity. At excitatory glutamatergic synapses, the immediate early gene product Arc/ Arg3.1 couples synaptic activity to postsynaptic endocytosis of AMPA-type glutamate receptors. Although the mechanisms for Arc induction have been described, little is known regarding the molecular machinery that terminates Arc function. Here, we demonstrate that the RING domain ubiquitin ligase Triad3A/RNF216 ubiquitinates Arc, resulting in its rapid proteasomal degradation. Triad3A associates with Arc, localizes to clathrin-coated pits, and is associated with endocytic sites in dendrites and spines. In the absence of Triad3A, Arc accumulates, leading to the loss of surface AMPA receptors. Furthermore, loss of Triad3A mimics and occludes Arc-dependent forms of synaptic plasticity. Thus, degradation of Arc by clathrin-localized Triad3A regulates the availability of synaptic AMPA receptors and temporally tunes Arc-mediated plasticity at glutamatergic synapses.Version
No full-text in the repositoryCitation
Mabb AM, Je HS, Wall MJ et al. (2014) Triad3A Regulates Synaptic Strength by Ubiquitination of Arc. Neuron, 82 (6): 1299–1316Link to Version of Record
https://doi.org/10.1016/j.neuron.2014.05.016Type
ArticleNotes
A final draft copy of this article is not yet available.ae974a485f413a2113503eed53cd6c53
https://doi.org/10.1016/j.neuron.2014.05.016